Neck-linker docking coordinates the kinetics of kinesin's heads.

ABSTRACT: Conventional kinesin is a two-headed homodimeric motor protein, which is able to walk along microtubules processively by hydrolyzing ATP. Its neck linkers, which connect the two motor domains and can undergo a docking/undocking transition, are widely believed to play the key role in the coordination of the chemical cycles of the two motor domains and, consequently, in force production and directional stepping. Although many experiments, often complemented with partial kinetic modeling of specific pathways, support this idea, the ultimate test of the viability of this hypothesis requires the construction of a complete kinetic model. Considering the two neck linkers as entropic springs that are allowed to dock to their head domains, and incorporating only the few most relevant kinetic and st

SUBMITTER: Czovek A 

PROVIDER: S-EPMC3072627 | biostudies-literature | 2011 Apr

REPOSITORIES: biostudies-literature